CDD_MOUSE
ID CDD_MOUSE Reviewed; 146 AA.
AC P56389; Q9D7V3;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Cytidine deaminase;
DE EC=3.5.4.5;
DE AltName: Full=Cytidine aminohydrolase;
GN Name=Cda; Synonyms=Cdd;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Stomach;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreas;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, and Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) IN COMPLEX WITH CYTIDINE, SUBUNIT,
RP COFACTOR, ACTIVE SITE, SUBSTRATE-BINDING REGION, AND ZINC-BINDING SITES.
RX PubMed=16784234; DOI=10.1021/bi060345f;
RA Teh A.H., Kimura M., Yamamoto M., Tanaka N., Yamaguchi I., Kumasaka T.;
RT "The 1.48 A resolution crystal structure of the homotetrameric cytidine
RT deaminase from mouse.";
RL Biochemistry 45:7825-7833(2006).
CC -!- FUNCTION: This enzyme scavenges exogenous and endogenous cytidine and
CC 2'-deoxycytidine for UMP synthesis. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cytidine + H(+) + H2O = NH4(+) + uridine;
CC Xref=Rhea:RHEA:16069, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16704, ChEBI:CHEBI:17562, ChEBI:CHEBI:28938; EC=3.5.4.5;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2'-deoxycytidine + H(+) + H2O = 2'-deoxyuridine + NH4(+);
CC Xref=Rhea:RHEA:13433, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15698, ChEBI:CHEBI:16450, ChEBI:CHEBI:28938; EC=3.5.4.5;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:16784234};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:16784234}.
CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC family. {ECO:0000305}.
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DR EMBL; AK008793; BAB25898.1; -; mRNA.
DR EMBL; BC050114; AAH50114.1; -; mRNA.
DR CCDS; CCDS18826.1; -.
DR RefSeq; NP_082452.1; NM_028176.1.
DR PDB; 1ZAB; X-ray; 2.36 A; A/B/C/D=1-146.
DR PDB; 2FR5; X-ray; 1.48 A; A/B/C/D=1-146.
DR PDB; 2FR6; X-ray; 2.07 A; A/B/C/D=1-146.
DR PDBsum; 1ZAB; -.
DR PDBsum; 2FR5; -.
DR PDBsum; 2FR6; -.
DR AlphaFoldDB; P56389; -.
DR SMR; P56389; -.
DR BioGRID; 215267; 3.
DR IntAct; P56389; 1.
DR MINT; P56389; -.
DR STRING; 10090.ENSMUSP00000030535; -.
DR BindingDB; P56389; -.
DR ChEMBL; CHEMBL2110; -.
DR iPTMnet; P56389; -.
DR PhosphoSitePlus; P56389; -.
DR jPOST; P56389; -.
DR MaxQB; P56389; -.
DR PaxDb; P56389; -.
DR PeptideAtlas; P56389; -.
DR PRIDE; P56389; -.
DR ProteomicsDB; 281351; -.
DR Antibodypedia; 29806; 322 antibodies from 30 providers.
DR DNASU; 72269; -.
DR Ensembl; ENSMUST00000030535; ENSMUSP00000030535; ENSMUSG00000028755.
DR GeneID; 72269; -.
DR KEGG; mmu:72269; -.
DR UCSC; uc008vkw.1; mouse.
DR CTD; 978; -.
DR MGI; MGI:1919519; Cda.
DR VEuPathDB; HostDB:ENSMUSG00000028755; -.
DR eggNOG; KOG0833; Eukaryota.
DR GeneTree; ENSGT00390000000911; -.
DR HOGENOM; CLU_097262_1_2_1; -.
DR InParanoid; P56389; -.
DR OMA; LTHFTCV; -.
DR OrthoDB; 1400471at2759; -.
DR PhylomeDB; P56389; -.
DR TreeFam; TF314486; -.
DR BRENDA; 3.5.4.5; 3474.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-73614; Pyrimidine salvage.
DR BioGRID-ORCS; 72269; 0 hits in 74 CRISPR screens.
DR ChiTaRS; Cda; mouse.
DR EvolutionaryTrace; P56389; -.
DR PRO; PR:P56389; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; P56389; protein.
DR Bgee; ENSMUSG00000028755; Expressed in right kidney and 83 other tissues.
DR Genevisible; P56389; MM.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0004126; F:cytidine deaminase activity; IDA:MGI.
DR GO; GO:0019239; F:deaminase activity; ISO:MGI.
DR GO; GO:0047844; F:deoxycytidine deaminase activity; IEA:RHEA.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0001882; F:nucleoside binding; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0071217; P:cellular response to external biotic stimulus; IEA:Ensembl.
DR GO; GO:0006248; P:CMP catabolic process; ISO:MGI.
DR GO; GO:0009972; P:cytidine deamination; ISS:UniProtKB.
DR GO; GO:0006249; P:dCMP catabolic process; ISO:MGI.
DR GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
DR GO; GO:0045980; P:negative regulation of nucleotide metabolic process; ISS:UniProtKB.
DR GO; GO:0046898; P:response to cycloheximide; IEA:Ensembl.
DR GO; GO:0044206; P:UMP salvage; IDA:MGI.
DR InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd.
DR InterPro; IPR002125; CMP_dCMP_dom.
DR InterPro; IPR006262; Cyt_deam_tetra.
DR InterPro; IPR016193; Cytidine_deaminase-like.
DR Pfam; PF00383; dCMP_cyt_deam_1; 1.
DR SUPFAM; SSF53927; SSF53927; 1.
DR TIGRFAMs; TIGR01354; cyt_deam_tetra; 1.
DR PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1.
DR PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..146
FT /note="Cytidine deaminase"
FT /id="PRO_0000171683"
FT DOMAIN 13..140
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT ACT_SITE 67
FT /note="Proton donor"
FT /evidence="ECO:0000269|PubMed:16784234"
FT BINDING 54..56
FT /ligand="substrate"
FT BINDING 65
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT BINDING 99
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT BINDING 102
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT HELIX 13..26
FT /evidence="ECO:0007829|PDB:2FR5"
FT TURN 32..34
FT /evidence="ECO:0007829|PDB:2FR5"
FT STRAND 38..44
FT /evidence="ECO:0007829|PDB:2FR5"
FT STRAND 49..53
FT /evidence="ECO:0007829|PDB:2FR5"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:2FR5"
FT HELIX 66..76
FT /evidence="ECO:0007829|PDB:2FR5"
FT STRAND 82..90
FT /evidence="ECO:0007829|PDB:2FR5"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:2FR5"
FT HELIX 100..108
FT /evidence="ECO:0007829|PDB:2FR5"
FT STRAND 114..118
FT /evidence="ECO:0007829|PDB:2FR5"
FT STRAND 124..128
FT /evidence="ECO:0007829|PDB:2FR5"
FT HELIX 129..132
FT /evidence="ECO:0007829|PDB:2FR5"
FT HELIX 139..142
FT /evidence="ECO:0007829|PDB:2FR5"
SQ SEQUENCE 146 AA; 16131 MW; D4181CE6BA9CD794 CRC64;
MAQERPSCAV EPEHVQRLLL SSREAKKSAY CPYSRFPVGA ALLTGDGRIF SGCNIENACY
PLGVCAERTA IQKAISEGYK DFRAIAISSD LQEEFISPCG ACRQVMREFG TDWAVYMTKP
DGTFVVRTVQ ELLPASFGPE DLQKIQ
